[NMR paper] Characterizing RNA dynamics at atomic resolution using solution-state NMR spectroscopy.
From Mendeley Biomolecular NMR group:
Characterizing RNA dynamics at atomic resolution using solution-state NMR spectroscopy.
Nature methods (2011). Volume: 8, Issue: 11. Pages: 919-31. Jameson R Bothe, Evgenia N Nikolova, Catherine D Eichhorn, Jeetender Chugh, Alexandar L Hansen, Hashim M Al-Hashimi et al.
Many recently discovered noncoding RNAs do not fold into a single native conformation but sample many different conformations along their free-energy landscape to carry out their biological function. Here we review solution-state NMR techniques that measure the structural,...
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10-12-2012 09:58 AM
[NMR paper] Characterizing RNA dynamics at atomic resolution using solution-state NMR spectroscopy.
From Mendeley Biomolecular NMR group:
Characterizing RNA dynamics at atomic resolution using solution-state NMR spectroscopy.
Nature methods (2011). Volume: 8, Issue: 11. Pages: 919-31. Jameson R Bothe, Evgenia N Nikolova, Catherine D Eichhorn, Jeetender Chugh, Alexandar L Hansen, Hashim M Al-Hashimi et al.
Many recently discovered noncoding RNAs do not fold into a single native conformation but sample many different conformations along their free-energy landscape to carry out their biological function. Here we review solution-state NMR techniques that measure the structural,...
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08-24-2012 08:01 PM
Dynamics of Biomolecules from Picoseconds to Seconds at Atomic Resolution
Dynamics of Biomolecules from Picoseconds to Seconds at Atomic Resolution
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 22 July 2011</br>
Dennis A., Torchia</br>
Although biomolecular dynamics has been investigated using NMR for at least 40 years, only in the past 20 years have internal motions been characterized at atomic resolution throughout proteins and nucleic acids. This development was made possible by multidimensional heteronuclear NMR approaches that provide near complete sequential signal assignments of...
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07-23-2011 10:40 PM
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy.
J Am Chem Soc. 2010 Oct 6;132(39):13765-75
Authors: Van Melckebeke H, Wasmer C, Lange A, Ab E, Loquet A, Böckmann A, Meier BH
We present a strategy to solve the high-resolution structure of amyloid fibrils by solid-state NMR and use it to determine the atomic-resolution structure of the prion domain of the fungal prion HET-s...
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01-21-2011 12:00 PM
[NMR paper] High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloi
High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Related Articles High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Angew Chem Int Ed Engl. 2005 Apr 15;44(16):2441-4
Authors: Siemer AB, Ritter C, Ernst M, Riek R, Meier BH
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11-25-2010 08:21 PM
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by So
Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy
He?le?ne Van Melckebeke, Christian Wasmer, Adam Lange, Eiso AB, Antoine Loquet, Anja Bo?ckmann and Beat H. Meier
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja104213j/aop/images/medium/ja-2010-04213j_0001.gif
Journal of the American Chemical Society
DOI: 10.1021/ja104213j
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qGRhA6CtOVc
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09-10-2010 12:48 AM
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution - Sec
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution - Securities Industry News (blog) (subscription)
<img alt="" height="1" width="1" />
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution
Securities Industry News (blog) (subscription)
In this work, we used chemical shifts and bond-vector orientation constraints obtained from nuclear magnetic resonance relaxation dispersion spectroscopy, ...
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09-10-2010 12:48 AM
[NMR paper] NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231
NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).
FEBS Lett. 1997 Aug 18;413(2):282-8
Authors: Riek R, Hornemann S, Wider G, Glockshuber R, Wüthrich K
The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling. NMR experiments showed that the previously...